Owlv2,1 Term Printed Access Card For Campbell/farrell/mcdougal's Biochemistry, 9th
9th Edition
ISBN: 9781305962972
Author: Campbell, Mary K.; Farrell, Shawn O.; Mcdougal, Owen M.
Publisher: Cengage Learning
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Chapter 7, Problem 47RE
REFLECT AND APPLY What properties of metal ions make them useful cofactors?
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The titration curve of alanine shows the ionization of two functional groups with pK values of 2.34 and 9.69, corresponding to
the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of
alanine also shows the ionization of only two functional groups, although the experimental pK values are different. The table
summarizes the trend in pK values.
Amino acid or peptide
Ala
Ala-Ala
pKj
pk₂
2.34
9.69
3.12
8.30
Ala-Ala-Ala
3.39
8.03
Ala-(Ala)-Ala, n ≥ 4
3.42
7.94
Modify the molecules to show the oligopeptide Ala-Ala-Ala. You can modify the molecules by moving, adding,
deleting, or changing atoms, bonds, or charges.
C
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c
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H с N 0
S
Cl
H
H
| | ||
H CH3
H
CH,
H CH₂
Complete the statements about the the pK, values of the Ala-Ala-Ala oligopeptide.
The pK₁ value of 3.39 is associated with the
-COO group of Ala-Ala-Ala.
The pK2 value of 8.03 is associated with the -NH
group of Ala-Ala-Ala.
Erase
Q2 Q…
Facts from the bacterium
mals and to dept kan apa
in a peptide with antidic properties. This peptide
complex with
the call membrance of other hacterial species, leading in bacterial death
The structure of the peptide has been determined from
(a) Cmplete acid hydes of the peptide, followed by amino acid analys, yielded quiar anunt of Lan, Om, Pfx, Prxa,
and Wall Cmtiti, an amino acid od prosentin pockets but present in some peptides. Com has the tracture
H
*H,N-CH-CH-CH, -C- COO
(b) The weight of the peptide in approximately 1,200 Th
(c) The peptide failed to undergo hydrolysis when treated with the
Hydrolysis of the carbonyl-terminal residue of a polypeptide une
"NH,
the
year. This call
there Pro or the police does not contain a froz
(d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and
ched only from and the derivative
NO,
Н
ON
NHCHI
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coo
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(Hint: The 2,4-diphenyl derivative involves the amino group of a side chain rather than the…
Electrophoresis
Macmillan Learning
Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a
single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and
lane 2 contains chymotrypsin pre-treated with performic acid.
1
2
Why does performic acid treatment of chymotrypsin generate three bands in lane 2?
°
Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues.
The three peptides are impurities in the original chymotrypsin sample.
Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues.
Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin.
Correct Answer
Chapter 7 Solutions
Owlv2,1 Term Printed Access Card For Campbell/farrell/mcdougal's Biochemistry, 9th
Ch. 7 - RECALL What features distinguish enzymes that...Ch. 7 - RECALL What is the metabolic role of aspartate...Ch. 7 - RECALL What molecule acts as a positive effector...Ch. 7 - RECALL Is the term KM used with allosteric...Ch. 7 - Prob. 5RECh. 7 - Prob. 6RECh. 7 - RECALL What is a homotropic effect? What is a...Ch. 7 - RECALL What is the structure of ATCase?Ch. 7 - RECALL How is the cooperative behavior of...Ch. 7 - RECALL Does the behavior of allosteric enzymes...
Ch. 7 - RECALL Does the behavior of allosteric enzymes...Ch. 7 - RECALL Explain what is meant by K0.5.Ch. 7 - REFLECT AND APPLY Explain the experiment used to...Ch. 7 - RECALL Distinguish between the concerted and...Ch. 7 - RECALL Which allosteric model can explain negative...Ch. 7 - RECALL With the concerted model, what conditions...Ch. 7 - Prob. 17RECh. 7 - Prob. 18RECh. 7 - Prob. 19RECh. 7 - Prob. 20RECh. 7 - Prob. 21RECh. 7 - BIOCHEMICAL CONNECTIONS How does Valium work?Ch. 7 - Prob. 23RECh. 7 - Prob. 24RECh. 7 - RECALL What is the function of a protein kinase?Ch. 7 - RECALL What amino acids are often phosphorylated...Ch. 7 - REFLECT AND APPLY What are some possible...Ch. 7 - REFLECT AND APPLY Explain how phosphorylation is...Ch. 7 - REFLECT AND APPLY Explain how glycogen...Ch. 7 - Prob. 30RECh. 7 - Prob. 31RECh. 7 - RECALL Name three proteins that are subject to the...Ch. 7 - Prob. 33RECh. 7 - RECALL What are caspases?Ch. 7 - REFLECT AND APPLY Explain why cleavage of the bond...Ch. 7 - REFLECT AND APPLY Why is it necessary or...Ch. 7 - Prob. 37RECh. 7 - Prob. 38RECh. 7 - Prob. 39RECh. 7 - RECALL What are the two essential amino acids in...Ch. 7 - RECALL Why does the enzyme reaction for...Ch. 7 - REFLECT AND APPLY Briefly describe the role of...Ch. 7 - REFLECT AND APPLY Explain the function of...Ch. 7 - REFLECT AND APPLY Explain why the second phase of...Ch. 7 - Prob. 45RECh. 7 - REFLECT AND APPLY An inhibitor that specifically...Ch. 7 - REFLECT AND APPLY What properties of metal ions...Ch. 7 - RECALL In biochemistry mechanisms, what group is...Ch. 7 - Prob. 49RECh. 7 - REFLECT AND APPLY Explain the difference between...Ch. 7 - Prob. 51RECh. 7 - Prob. 52RECh. 7 - Prob. 53RECh. 7 - REFLECT AND APPLY What is the relationship between...Ch. 7 - Prob. 55RECh. 7 - BIOCHEMICAL CONNECTIONS Why can cocaine addiction...Ch. 7 - Prob. 57RECh. 7 - Prob. 58RECh. 7 - RECALL How are coenzymes related to vitamins?Ch. 7 - RECALL What type of reaction uses vitamin B6?Ch. 7 - Prob. 61RECh. 7 - Prob. 62RECh. 7 - Prob. 63RECh. 7 - BIOCHEMICAL CONNECTIONS What are some of the ways...Ch. 7 - Prob. 65RECh. 7 - Prob. 66RECh. 7 - Prob. 67RECh. 7 - Prob. 68RECh. 7 - Prob. 69RECh. 7 - Prob. 70RECh. 7 - Prob. 71RECh. 7 - Prob. 72RECh. 7 - Prob. 73RE
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- Extracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death. The structure of the peptide has been determined from a series of observations. (a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure H 'H,N-CH, - CH2 CH2 CH2 - C - COO- NH, (b) The molecular weight of the peptide is approximately 1,200 Da. (c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free carboxyl group. (d) Treatment of the intact peptide with…arrow_forwardAt a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pl is zwitterionic. CH3 H,N CH3 ** H¸N-C H Zwitterionic H Uncharged OH Select statements that explain why alanine is predominantly zwitterionic at its pl. pk of alanine's amino group is more than its pl. pk of alanine's carboxyl group is more than its pl. PK of alanine's carboxyl group is less than its pl. pk of alanine's amino group is less than its pl. Correct Answer What fraction of alanine is in the completely uncharged form at its pl? 1 in 2.2 × 107 1 in 1.6 × 10² 1 in 4680 1 in 9460arrow_forwardHow does a voltage-gated sodium channel work? Specifically, how and why does a change in voltage trigger their opening? Please be detailedarrow_forward
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